z-logo
open-access-imgOpen Access
Nuclease-T: an active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragments.
Author(s) -
Hiroshi Taniuchi,
Christian B. Anfinsen,
Ann Sodja
Publication year - 1967
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.58.3.1235
Subject(s) - nuclease , quantum , physics , symmetry (geometry) , interpretation (philosophy) , quantum mechanics , theoretical physics , mathematics , computer science , geometry , nuclear magnetic resonance , enzyme , programming language
This is one of many articles produced by Anfinsen's research team and others on the factors contributing to the translation of the genetic message for a particular protein backbone. Taniuchi, Sodja, and Anfinsen determined that such a translation was no longer possible if the linear information had been manipulated through the deletion of amino acid residues. However, they did find that some proteins that they termed "recombining systems" could be cleaved into two, or even three, fragments that recombined through non-covalent forces to yield biologically active structures with physical properties very similar to those of the parent protein molecules.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom